PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15956117-4 2005 Phosphoramidon, a dual neutral endopeptidase and endothelin-converting enzyme inhibitor, blocked both pressor responses to endothelin-1 (1-31) and big endothelin-1 but not those afforded by endothelin-1. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 123-135 15956117-4 2005 Phosphoramidon, a dual neutral endopeptidase and endothelin-converting enzyme inhibitor, blocked both pressor responses to endothelin-1 (1-31) and big endothelin-1 but not those afforded by endothelin-1. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 151-163 15956117-4 2005 Phosphoramidon, a dual neutral endopeptidase and endothelin-converting enzyme inhibitor, blocked both pressor responses to endothelin-1 (1-31) and big endothelin-1 but not those afforded by endothelin-1. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 151-163 15956117-7 2005 Furthermore, injection of big endothelin-1 concomitantly with phosphoramidon induced an increase in endothelin-1 (1-31) plasma levels. phosphoramidon 62-76 endothelin-1 Oryctolagus cuniculus 30-42 15956117-7 2005 Furthermore, injection of big endothelin-1 concomitantly with phosphoramidon induced an increase in endothelin-1 (1-31) plasma levels. phosphoramidon 62-76 endothelin-1 Oryctolagus cuniculus 100-112 15956117-8 2005 Finally, intracardiac-administered endothelin-1 (1-31) induced an increase of endothelin-1 plasma levels, which are markedly reduced by phosphoramidon and thiorphan but not by CGS 35066. phosphoramidon 136-150 endothelin-1 Oryctolagus cuniculus 35-47 15956117-8 2005 Finally, intracardiac-administered endothelin-1 (1-31) induced an increase of endothelin-1 plasma levels, which are markedly reduced by phosphoramidon and thiorphan but not by CGS 35066. phosphoramidon 136-150 endothelin-1 Oryctolagus cuniculus 78-90 7896062-3 1994 Addition of phosphoramidon to the medium caused a potentiation in the vasoconstrictor response to endothelin-1 and greatly, but not completely, inhibited vasoconstriction induced by pre-pro-endothelin-1. phosphoramidon 12-26 endothelin-1 Oryctolagus cuniculus 98-110 8938666-3 1996 The metalloprotease inhibitor phosphoramidon (30 mumol/l) almost abolished the contractile response to big ET-1, whereas the ET-1-induced contraction was unaffected. phosphoramidon 30-44 endothelin-1 Oryctolagus cuniculus 107-111 8938666-9 1996 These results suggest that externally applied big ET-1 is converted to ET-1 by a phosphoramidon-sensitive "endothelin converting enzyme" present in the vascular smooth muscle cells. phosphoramidon 81-95 endothelin-1 Oryctolagus cuniculus 50-54 8938666-9 1996 These results suggest that externally applied big ET-1 is converted to ET-1 by a phosphoramidon-sensitive "endothelin converting enzyme" present in the vascular smooth muscle cells. phosphoramidon 81-95 endothelin-1 Oryctolagus cuniculus 71-75 12099999-9 2002 This increase is attributed to the higher conversion rate of big ET-1 to ET-1 because the ET-converting enzyme (ECE) inhibitor phosphoramidon, at a concentration of 10(-6) mol/L, causes an inhibition in the response to big ET-1 by 52.6% in normal kidneys, whereas this inhibition with the same concentration of phosphoramidon was found to be significantly decreased in kidneys isolated from GLY-pretreated rabbits. phosphoramidon 127-141 endothelin-1 Oryctolagus cuniculus 65-77 12099999-9 2002 This increase is attributed to the higher conversion rate of big ET-1 to ET-1 because the ET-converting enzyme (ECE) inhibitor phosphoramidon, at a concentration of 10(-6) mol/L, causes an inhibition in the response to big ET-1 by 52.6% in normal kidneys, whereas this inhibition with the same concentration of phosphoramidon was found to be significantly decreased in kidneys isolated from GLY-pretreated rabbits. phosphoramidon 127-141 endothelin-1 Oryctolagus cuniculus 65-69 12099999-9 2002 This increase is attributed to the higher conversion rate of big ET-1 to ET-1 because the ET-converting enzyme (ECE) inhibitor phosphoramidon, at a concentration of 10(-6) mol/L, causes an inhibition in the response to big ET-1 by 52.6% in normal kidneys, whereas this inhibition with the same concentration of phosphoramidon was found to be significantly decreased in kidneys isolated from GLY-pretreated rabbits. phosphoramidon 311-325 endothelin-1 Oryctolagus cuniculus 65-77 12099999-9 2002 This increase is attributed to the higher conversion rate of big ET-1 to ET-1 because the ET-converting enzyme (ECE) inhibitor phosphoramidon, at a concentration of 10(-6) mol/L, causes an inhibition in the response to big ET-1 by 52.6% in normal kidneys, whereas this inhibition with the same concentration of phosphoramidon was found to be significantly decreased in kidneys isolated from GLY-pretreated rabbits. phosphoramidon 311-325 endothelin-1 Oryctolagus cuniculus 65-69 10720586-9 2000 Finally, systemically administered big ET-1, but not big ET-2, induced a phosphoramidon-sensitive increase in plasma IR-ET. phosphoramidon 73-87 endothelin-1 Oryctolagus cuniculus 39-43 10374426-12 1998 L-NMA and phosphoramidon obviously reduced the plasma levels of NO and ET-1 to below their respective baseline levels, and showed transient effect of increase on blood pressure. phosphoramidon 10-24 endothelin-1 Oryctolagus cuniculus 71-75 7896062-13 1994 From these results it was concluded that phosphoramidon-sensitive endothelin-converting enzyme, probably localized in microvasculature of the kidney, can convert pre-pro-endothelin-1 to endothelin-1 which is responsible for the vasoconstrictor effect of pre-pro-endothelin-1 in addition to its possible direct vasoconstrictor effect on kidney vasculature. phosphoramidon 41-55 endothelin-1 Oryctolagus cuniculus 170-182 7896062-13 1994 From these results it was concluded that phosphoramidon-sensitive endothelin-converting enzyme, probably localized in microvasculature of the kidney, can convert pre-pro-endothelin-1 to endothelin-1 which is responsible for the vasoconstrictor effect of pre-pro-endothelin-1 in addition to its possible direct vasoconstrictor effect on kidney vasculature. phosphoramidon 41-55 endothelin-1 Oryctolagus cuniculus 186-198 7896062-13 1994 From these results it was concluded that phosphoramidon-sensitive endothelin-converting enzyme, probably localized in microvasculature of the kidney, can convert pre-pro-endothelin-1 to endothelin-1 which is responsible for the vasoconstrictor effect of pre-pro-endothelin-1 in addition to its possible direct vasoconstrictor effect on kidney vasculature. phosphoramidon 41-55 endothelin-1 Oryctolagus cuniculus 186-198 7896062-3 1994 Addition of phosphoramidon to the medium caused a potentiation in the vasoconstrictor response to endothelin-1 and greatly, but not completely, inhibited vasoconstriction induced by pre-pro-endothelin-1. phosphoramidon 12-26 endothelin-1 Oryctolagus cuniculus 190-202 1451739-0 1992 The vasoconstrictor action of big endothelin-1 is phosphoramidon-sensitive in rabbit saphenous artery, but not in saphenous vein. phosphoramidon 50-64 endothelin-1 Oryctolagus cuniculus 34-46 7510001-7 1993 Phosphoramidon (10 microM) infused TK blocked (92 +/- 1% inhibition) the renal responses to bET-1 and reduced the overflow of ET-1-like material onto the tissues without affecting ET-1-induced renal vasoconstriction. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 93-97 7510001-7 1993 Phosphoramidon (10 microM) infused TK blocked (92 +/- 1% inhibition) the renal responses to bET-1 and reduced the overflow of ET-1-like material onto the tissues without affecting ET-1-induced renal vasoconstriction. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 126-130 7510001-8 1993 Incubation of bET-1 with rabbit renal cortical microsomes (100 micrograms protein) resulted in the generation of ET-1-like activity, as assessed by bioassay, which was inhibited by phosphoramidon (10 microM). phosphoramidon 181-195 endothelin-1 Oryctolagus cuniculus 15-19 1451739-4 1992 Phosphoramidon (100 microM), a metalloproteinase inhibitor, antagonised the contractile action of big endothelin-1 in the artery but not in the vein. phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 102-114 1398887-5 1992 A metalloprotease inhibitor, phosphoramidon (100 microM, 60 minutes), reduced the prostanoid release and pressor responses induced by big endothelin-1 and -2 without affecting the response induced by endothelin-1, -2, and -3. phosphoramidon 29-43 endothelin-1 Oryctolagus cuniculus 138-157 1398887-6 1992 These results suggest the presence of a phosphoramidon-sensitive endothelin converting enzyme that converts the precursors of endothelin-1 and -2, but not of endothelin-3, in the renal vasculature of the rabbit. phosphoramidon 40-54 endothelin-1 Oryctolagus cuniculus 126-145 1629095-7 1992 Phosphoramidon, an inhibitor of metalloproteinase, suppressed the pressor effect of big ET-1 (P less than 0.01) and the increase in the concentration of ET-1 in the perfusate (P less than 0.05). phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 88-92 1629095-7 1992 Phosphoramidon, an inhibitor of metalloproteinase, suppressed the pressor effect of big ET-1 (P less than 0.01) and the increase in the concentration of ET-1 in the perfusate (P less than 0.05). phosphoramidon 0-14 endothelin-1 Oryctolagus cuniculus 153-157